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A critical evaluation of the predicted and X-ray structures of α-Lactalbumin

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Abstract

The rapidly increasing availability of protein amino-acid sequences, many of which have been determined from the corresponding gene sequences, has intensified interest in the prediction of related protein structures when the three-dimensional structure of another member of the family is known. The study of bovine α-Lactalbumin provides a classic example in which the three-dimensional structure was predicted, first by Browneet al. (1969) and later by Warmeet al. (1974), from the three-dimensional structure of hen-egg-white lysozyme (Blakeet al., 1965), taking into account the striking relationship between the amino acid sequences of the two proteins. A comprehensive comparison of these models with the structure of baboon α-Lactalbumin derived from X-ray crystallography (Acharyaet al., 1989) is presented. The models mostly compare well with the experimentally determined structure except in the flexible C-terminal region of the molecule (rms deviation on Cα of residues 1–95, 1.1 Å).

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Authors and Affiliations

  1. Laboratory of Molecular Biophysics, University of Oxford, The Rex Richards Building, South Parks Road, OX1 3QU, Oxford, England

    K. Ravi Acharya, David I. Stuart & David C. Phillips

  2. Baker Laboratory of Chemistry, Cornell University, 14853-1301, Ithaca, New York

    Harold A. Scheraga

  3. Department of Biochemistry, University of Bath, BA2 7AY, Claverton Down, Bath, England

    K. Ravi Acharya

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  1. K. Ravi Acharya
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  4. Harold A. Scheraga
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Acharya, K.R., Stuart, D.I., Phillips, D.C. et al. A critical evaluation of the predicted and X-ray structures of α-Lactalbumin. J Protein Chem 9, 549–563 (1990). https://doi.org/10.1007/BF01025008

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